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Literature summary extracted from
- Pericyclic reactions catalyzed by chorismate-utilizing enzymes (2011), Biochemistry, 50, 7476-7483.
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.4.4.2 | Mg2+ | required, chelated by residues D310, E313, and H348 | Pseudomonas aeruginosa |  |
| 5.4.99.5 | additional information | chorismate mutase activity is only detected when the Mg2+ is not present in the wild-type active site | Pseudomonas aeruginosa |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.99.21 | isochorismate | Pseudomonas aeruginosa | - |
salicylate + pyruvate | - |
? | |
| 5.4.4.2 | Chorismate | Pseudomonas aeruginosa | - |
Isochorismate | - |
r | |
| 5.4.99.5 | Chorismate | Pseudomonas aeruginosa | - |
Prephenate | - |
? | |
| 5.4.99.5 | additional information | Pseudomonas aeruginosa | isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform the chorismate mutase reaction | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.99.21 | Pseudomonas aeruginosa | - |
gene pchB | - |
| 5.4.4.2 | Pseudomonas aeruginosa | - |
- |
- |
| 5.4.99.5 | Pseudomonas aeruginosa | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.2.99.21 | isochorismate = salicylate + pyruvate | reaction mechanism with catalytic residue Lys42, modeling, overview | Pseudomonas aeruginosa | |
| 5.4.99.5 | Chorismate = prephenate | via near attack conformation and transition state intermediates, reaction mechanism, overview | Pseudomonas aeruginosa |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.99.21 | isochorismate | - |
Pseudomonas aeruginosa | salicylate + pyruvate | - |
? | |
| 4.2.99.21 | isochorismate | elimination of pyruvate | Pseudomonas aeruginosa | salicylate + pyruvate | - |
? | |
| 4.2.99.21 | additional information | PchB can also perform a nonphysiological role as a chorismate mutase, EC 4.1.3.40, albeit with considerably lower catalytic efficiency | Pseudomonas aeruginosa | ? | - |
? | |
| 5.4.4.2 | Chorismate | - |
Pseudomonas aeruginosa | Isochorismate | - |
r | |
| 5.4.99.5 | Chorismate | - |
Pseudomonas aeruginosa | Prephenate | - |
? | |
| 5.4.99.5 | additional information | isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform the chorismate mutase reaction | Pseudomonas aeruginosa | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.4.99.5 | More | enzyme structure comparisons of isochorismate-pyruvate lyase, PchB, with chorismate mutases, overview | Pseudomonas aeruginosa |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.2.99.21 | isochorismate-pyruvate lyase | - |
Pseudomonas aeruginosa |
| 4.2.99.21 | PchB | - |
Pseudomonas aeruginosa |
| 5.4.4.2 | PchA | - |
Pseudomonas aeruginosa |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.2.99.21 | evolution | PchB is a structural homologue of the AroQ chorismate mutases | Pseudomonas aeruginosa |
| 4.2.99.21 | metabolism | the enzyme is involved in siderophore pyochelin via salicylate biosynthesis | Pseudomonas aeruginosa |
| 4.2.99.21 | additional information | structure-function relationship, biocatalysis of pericyclic reactions, overview. For PchB, the pericyclic reaction is a concerted but asynchronous [1,5]-sigmatropic shift with a quantitative transfer of hydrogen from C2 to C9. Major structural difference between the apo form and the pyruvate-bound or the pyruvate-and salicylate-bound forms of PchB: the active site loop between helix 1 and helix 2 is disordered in the apo structure but fully ordered in the ligand-bound structures. The difference between the open and closed structures is due to a conserved active site lysine 42, which hydrogen bonds to a bound pyruvate molecule. Quantum mechanical/molecular mechanical molecular dynamics simulations, overview | Pseudomonas aeruginosa |
| 5.4.4.2 | metabolism | the enzyme produces isochorismate for conversion to salicylate by isochorismate-pyruvate lyase, PchB, and incorporation into the pyochelin siderophore. Isochorismate synthase (PchA) and isochorismate-pyruvate lyase (PchB) from Pseudomonas aeurginosa are involved in the synthesis of the siderophore pyochelin | Pseudomonas aeruginosa |
| 5.4.4.2 | additional information | structure-function relationships of chorismate-utilizing enzymes, structure comparisons, overview. Isochorismate synthase cannot perform any pericyclic reaction. Residues K221 and E269 are general base and acid, respectively | Pseudomonas aeruginosa |
| 5.4.99.5 | additional information | structure-function relationships of chorismate-utilizing enzymes, structure comparisons, overview | Pseudomonas aeruginosa |
| 5.4.99.5 | physiological function | isochorismate-pyruvate lyase, PchB EC 4.2.99.21, can also perform a nonphysiological role as a chorismate mutase albeit with considerably lower catalytic efficiency | Pseudomonas aeruginosa |
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